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JBC, Vol. 270, Issue 19, 11216-11221, May, 1995
JH Leusen, K Fluiter, PM Hilarius, D Roos, AJ Verhoeven and BG Bolscher
Activation of the human NADPH oxidase requires the interaction of at least
four cytosolic proteins and one membrane-bound heterodimeric protein. Src
homology 3 (SH3) domains and their proline-rich counterstructures have been
shown to play an important role in protein- protein interactions. Because
it was found that the cytosolic oxidase components p67phox, p47phox, and
p40phox reside in a complex in resting neutrophils, we studied the role of
SH3 domains in their interaction by use of an overlay technique. Wild-type
and mutated 35S-labeled p67phox and p47phox were used to detect immobilized
cytosolic proteins on a protein blot. A specific association of native
p67phox to blotted p47phox and blotted p40phox was found. These
interactions were not disturbed by deleting the only proline-rich region
(amino acids 227- 231) in p67phox. We also found a specific association of
native p47phox with blotted p67phox. Deletions in a putative SH3-binding
region of p47phox completely abrogated the interaction with p67phox. Other
results suggest that the C terminus of p47phox exposes this SH3-binding
domain for interaction with p67phox. Similar results were obtained when the
binding of cytosolic p67phox to wild-type or mutated p47phox were studied
in solution. Interestingly, mutants of p47phox unable to bind to p67phox
were fully capable of supporting superoxide production under cell-free
activation conditions. We conclude that an interaction between the
C-terminal proline-rich region of p47phox and the second SH3 domain of
p67phox is not required for oxidase activity in the cell- free assay.
Interactions between the cytosolic components p47phox and p67phox of the human neutrophil NADPH oxidase that are not required for activation in the cell-free system
Central Laboratory of the Netherlands Red Cross Blood Transfusion Service, Amsterdam.
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